1bru

STRUCTURE OF PORCINE PANCREATIC ELASTASE COMPLEXED WITH THE ELASTASE INHIBITOR GR143783

Method: X-RAY DIFFRACTION D_max: 54.2 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

ELASTASE

OrganismNot specified

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain P； UniProt 29–269	Not recorded	1NB 2-(2-HYDROXY-CYCLOPENTYL)-PENT-4-ENAL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 5；pH 5.0	Resolution 2.30 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	ELA2_PIG
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain P； PDBConstruct 1–241； UniProt 29–269

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1bru
Deposition date deposition_date	1998-08-24
Structure title title	STRUCTURE OF PORCINE PANCREATIC ELASTASE COMPLEXED WITH THE ELASTASE INHIBITOR GR143783
Keywords keywords	SERINE PROTEASE, HYDROLASE; SERINE PROTEASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	17.76 Å
Radius of gyration Rg (electron density) rg_electron	16.62 Å
Forward intensity I(0) i0	12784600.00
Molecular weight molecular_weight	25997.0 kDa
Excluded volume excluded_volume	32176 Å³
Envelope volume envelope_volume	35965 Å³
Hydration-shell volume shell_volume	17743 Å³
Envelope diameter envelope_diameter	54.5 Å
Shell Rg shell_rg	23.10 Å
Envelope Rg envelope_rg	16.85 Å
Shape Rg shape_rg	16.62 Å
Total Rg total_rg	17.59 Å
Total atoms total_atoms	1829
Residues n_residues	241
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	54.2 Å
Rg (real space) rg_real	17.61 Å
Rg uncertainty (real space) rg_real_error	0.31 Å
I(0) (real space) i0_real	1.2780e+07
I(0) uncertainty (real space) i0_real_error	1.4640e+05
Rg (reciprocal space) rg_reciprocal	17.63 Å
I(0) (reciprocal space) i0_reciprocal	12780000.0000
Solution quality estimate total_estimate	0.7794
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	6
Primary peak position r_peak_primary	21.7 Å
Skewness Skewness skewness	0.074
Kurtosis Kurtosis kurtosis	-0.456
Angular range angular_range	— – 0.4500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2936000.0000
Real-space data points n_real_points	76
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.771; Stabil: 0.942; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1brup_
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.2 — Eukaryotic proteases

CATH v4.4 (2 domains)

Domain ID domain_id	1bruP01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	1bruP02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

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8. Citations (1)

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Unit-cell length a length_a	41.590 Å
Unit-cell length b length_b	46.450 Å
Unit-cell length c length_c	128.230 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.1470
R_work r_work	0.1470
R_free r_free	—

Description description	ELASTASE
Molecular weight formula_weight	25847.9 kDa
EC 编号 ec_number	3.4.21.71
Source method src_method	nat
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	P
Atom count atom_count	2023

STRUCTURE OF PORCINE PANCREATIC ELASTASE COMPLEXED WITH THE ELASTASE INHIBITOR GR143783

1. Protein Identity and Related Structures Protein Identity & Related Structures

ELASTASE

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	2-(2-HYDROXY-CYCLOPENTYL)-PENT-4-ENAL
Molecular weight formula_weight	168.2 kDa
Source method src_method	syn
Copy count entity_count	1

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	194

fit	/app/data/saxs_computation/br/1bru/1bru.fit
pddf	/app/data/pr_computation/br/1bru/1bru.pr.out
profile	/app/data/saxs_computation/br/1bru/1bru.dat